Structure of PDB 2xyl Chain A Binding Site BS01

Receptor Information
>2xyl Chain A (length=312) Species: 1708 (Cellulomonas fimi) [Search protein sequence] [Download receptor structure] [Download structure with residue number starting from 1] [View receptor structure]
ATTLKEAADGAGRDFGFALDPNRLSEAQYKAIADSEFNLVVAENAMKWDA
TEPSQNSFSFGAGDRVASYAADTGKELYGHTLVWHSQLPDWAKNLNGSAF
ESAMVNHVTKVADHFEGKVASWDVVNEAFADGGGRRQDSAFQQKLGNGYI
ETAFRAARAADPTAKLCINDYNVEGINAKSNSLYDLVKDFKARGVPLDCV
GFQSHLIVGQVPGDFRQNLQRFADLGVDVRITELDIRMRTPSDATKLATQ
AADYKKVVQACMQVTRCQGVTVWGITDKYSWVPDVFPGEGAALVWDASYA
KKPAYAAVMEAF
Ligand information
Ligand IDX2F
InChIInChI=1S/C5H9FO4/c6-3-4(8)2(7)1-10-5(3)9/h2-5,7-9H,1H2/t2-,3-,4+,5+/m1/s1
InChIKeyYVMHSZGJGHRGOD-MBMOQRBOSA-N
SMILES
SoftwareSMILES
CACTVS 3.341O[CH]1CO[CH](O)[CH](F)[CH]1O
OpenEye OEToolkits 1.5.0C1[C@H]([C@@H]([C@H]([C@H](O1)O)F)O)O
OpenEye OEToolkits 1.5.0C1C(C(C(C(O1)O)F)O)O
CACTVS 3.341O[C@@H]1CO[C@H](O)[C@H](F)[C@H]1O
ACDLabs 10.04FC1C(O)C(O)COC1O
FormulaC5 H9 F O4
Name2-deoxy-2-fluoro-alpha-D-xylopyranose;
2-DEOXY-2-FLUORO XYLOPYRANOSE;
2-deoxy-2-fluoro-alpha-D-xylose;
2-deoxy-2-fluoro-D-xylose;
2-deoxy-2-fluoro-xylose
ChEMBL
DrugBank
ZINC
PDB chain2xyl Chain B Residue 1 [Download ligand structure] [Download structure with residue number starting from 1] [View ligand structure]
Receptor-Ligand Complex Structure
Global viewLocal viewStructure summary

[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
[Spin on] [Spin off] [Reset]
[High quality] [Low quality]
[White background] [Black background]
PDB2xyl Exploring the cellulose/xylan specificity of the beta-1,4-glycanase cex from Cellulomonas fimi through crystallography and mutation.
Resolution1.9 Å
Binding residue
(original residue number in PDB)		K47 H80 W84 Q203 H205 E233 W273 W281
Binding residue
(residue number reindexed from 1)		K47 H80 W84 Q203 H205 E233 W273 W281
Annotation score1
Enzymatic activity
Catalytic site (original residue number in PDB) E127 N169 H205 E233 D235
Catalytic site (residue number reindexed from 1) E127 N169 H205 E233 D235
Enzyme Commision number 3.2.1.8: endo-1,4-beta-xylanase.
3.2.1.91: cellulose 1,4-beta-cellobiosidase (non-reducing end).
Gene Ontology
Molecular Function
GO:0004553 hydrolase activity, hydrolyzing O-glycosyl compounds
Biological Process
GO:0005975 carbohydrate metabolic process

View graph for
Molecular Function
View graph for
Biological Process
External links
PDB RCSB:2xyl, PDBe:2xyl, PDBj:2xyl
PDBsum2xyl
PubMed9537990
UniProtP07986|GUX_CELFI Exoglucanase/xylanase (Gene Name=cex)

[Back to BioLiP]